Article citationsMore>>

Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S. (2001) Biochemical Characterization of Acyl Carrier Protein (AcpM) and Malonyl-CoA: AcpM Transacylase (mtFabD), Two Major Components of Mycobacterium tuberculosis Fatty Acid Synthase II. The Journal of Biological Chemistry, 276, 27967-27974.
http://dx.doi.org/10.1074/jbc.M103687200

has been cited by the following article:

• TITLE: Cloning and Enzymatic Activity Analysis of the Malonyl-CoA:acyl Carrier Protein Transacylase in Brassica napus Cultivars with Different Oil Content

  AUTHORS: Chenning Qu, Huanhuan Jiang, Lei Zhang

  KEYWORDS: Malonyl-CoA:acyl Carrier Protein Transacylase (MCAT), Brassica Napus, Oil Content, Relative Activities

  JOURNAL NAME: American Journal of Plant Sciences, Vol.5 No.18, August 7, 2014

  ABSTRACT: The full-length genomic DNA of MCAT (Malonyl-CoA:acyl carrier protein transacylase) in Brassica napus was cloned. BnMCAT shares very high identity with AtMCAT in gene sequence and gene structure. A multiple alignment of the protein sequence showed that BnMCAT shares high identity with other MCATs from E. coli and plants. BnMCAT was expressed in all tissues, such as roots, stems, leaves, flowers, and seeds, and no significant differences in the expression level were found in different embryo stages after pollination. According to an in vitro relative activity analysis, purified recombinant BnMCAT expressed in E. coli had transacylase activity. Although the relative activities of BnMCAT in crude extracts isolated from different staged embryos were similar and showed little variation, a higher relative activity was found in a crude extract isolated from embryos in comparison to leaves. Different relative activities of BnMCAT in crude extracts isolated from cultivars with different oil content were also found, suggesting that the activity of BnMCAT might be a decisive factor for a high oil content. Together, these results showed that BnMCAT is an important enzyme in the FAS system and indicate that BnMCAT might be a new target enzyme for future crop improvement through genetic engineering.